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Volumn 369, Issue 1, 2003, Pages 117-128

Agonist-induced changes in the phosphorylation of the myosin-binding subunit of myosin light chain phosphatase and CPI17, two regulatory factors of myosin light chain phosphatase, in smooth muscle

Author keywords

Histamine; Myosin phosphorylation; Protein kinase C; Rho associated kinase; Smooth muscle contraction

Indexed keywords

ANTIBODIES; MUSCLE; PROTEINS;

EID: 0037270157     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021040     Document Type: Article
Times cited : (109)

References (48)
  • 1
    • 0001068154 scopus 로고
    • Biochemistry of the contractile process in smooth muscle
    • (Johnson, L. R., ed.). Raven Press, New York
    • Hartshorne, D. J. (1987) Biochemistry of the contractile process in smooth muscle. In Physiology of the Gastrointestinal Tract, vol. 1 (Johnson, L. R., ed.), pp. 423-482, Raven Press, New York
    • (1987) Physiology of the Gastrointestinal Tract , vol.1 , pp. 423-482
    • Hartshorne, D.J.1
  • 2
    • 0024550123 scopus 로고
    • Regulation of smooth muscle contractile elements by second messengers
    • Kamm, K. E. and Stull, J. T. (1989) Regulation of smooth muscle contractile elements by second messengers. Annu. Rev. Physiol. 51, 299-313
    • (1989) Annu. Rev. Physiol. , vol.51 , pp. 299-313
    • Kamm, K.E.1    Stull, J.T.2
  • 3
    • 0026709998 scopus 로고
    • Control of nonmuscle myosins by phosphorylation
    • Tan, J. L., Ravid, S. and Spudich, J. A. (1992) Control of nonmuscle myosins by phosphorylation. Annu. Rev. Biochem. 61, 721-759
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 721-759
    • Tan, J.L.1    Ravid, S.2    Spudich, J.A.3
  • 4
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • Somlyo, A. P. and Somlyo, A. V. (1994) Signal transduction and regulation in smooth muscle. Nature (London) 372, 231-236
    • (1994) Nature (London) , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 5
    • 0021287453 scopus 로고
    • Stimulus-specific patterns of intracellular calcium levels in smooth muscle of ferret portal vein
    • Morgan, J. P. and Morgan, K. G. (1984) Stimulus-specific patterns of intracellular calcium levels in smooth muscle of ferret portal vein. J. Physiol. 351, 155-167
    • (1984) J. Physiol. , vol.351 , pp. 155-167
    • Morgan, J.P.1    Morgan, K.G.2
  • 6
    • 0023820267 scopus 로고
    • 2+] determines myosin phosphorylation in agonist-stimulated swine arterial smooth muscle
    • 2+] determines myosin phosphorylation in agonist-stimulated swine arterial smooth muscle. Circ. Res. 63, 593-603
    • (1988) Circ. Res. , vol.63 , pp. 593-603
    • Rembold, C.M.1    Murphy, R.A.2
  • 7
    • 0023805629 scopus 로고
    • 2+-tension relationship in vascular smooth muscle of rat aorta
    • 2+-tension relationship in vascular smooth muscle of rat aorta. Eur. J. Pharmacol. 151, 325-328
    • (1988) Eur. J. Pharmacol. , vol.151 , pp. 325-328
    • Karaki, H.1    Sato, K.2    Ozaki, H.3
  • 8
    • 0024826080 scopus 로고
    • Aequorin luminescence, myosin phosphorylation, and active stress in tracheal smooth muscle
    • Gerthoffer, W. T., Murphey, K. A. and Gunst, S. J. (1989) Aequorin luminescence, myosin phosphorylation, and active stress in tracheal smooth muscle. Am. J. Physiol. 257, C1062-C1068
    • (1989) Am. J. Physiol. , vol.257
    • Gerthoffer, W.T.1    Murphey, K.A.2    Gunst, S.J.3
  • 11
    • 0026692912 scopus 로고
    • Myosin light chain phosphatase activities and the effects of phosphatase inhibitors in tonic and phasic smooth muscle
    • Gong, M. C., Cohen, P., Kitazawa, T., Ikebe, M., Masuo, M., Somlyo, A. P. and Somlyo, A. V. (1992) Myosin light chain phosphatase activities and the effects of phosphatase inhibitors in tonic and phasic smooth muscle. J. Biol. Chem. 267, 14662-14668
    • (1992) J. Biol. Chem. , vol.267 , pp. 14662-14668
    • Gong, M.C.1    Cohen, P.2    Kitazawa, T.3    Ikebe, M.4    Masuo, M.5    Somlyo, A.P.6    Somlyo, A.V.7
  • 12
    • 0026048788 scopus 로고
    • G protein-mediated inhibition of myosin light-chain phosphatase in vascular smooth muscle
    • Kitazawa, T., Masuo, M. and Somlyo, A. P. (1991) G protein-mediated inhibition of myosin light-chain phosphatase in vascular smooth muscle. Proc. Natl. Acad. Sci. U.S.A. 88, 9307-9310
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9307-9310
    • Kitazawa, T.1    Masuo, M.2    Somlyo, A.P.3
  • 13
    • 0028168041 scopus 로고
    • 2+-sensitizing effect of protein kinase C on vascular smooth muscle: Inhibition of myosin light chain phosphatase
    • 2+-sensitizing effect of protein kinase C on vascular smooth muscle: inhibition of myosin light chain phosphatase. J. Gen. Physiol. 104, 265-286
    • (1994) J. Gen. Physiol. , vol.104 , pp. 265-286
    • Masuo, M.1    Reardon, S.2    Ikebe, M.3    Kitazawa, T.4
  • 14
    • 0030583303 scopus 로고    scopus 로고
    • Protein kinase C increases force and slows relaxation in smooth muscle: Evidence for regulation of the myosin light chain phosphatase
    • Ikebe, M. and Brozovich, F. V. (1996) Protein kinase C increases force and slows relaxation in smooth muscle: evidence for regulation of the myosin light chain phosphatase. Biochem. Biophys. Res. Commun. 225, 370-376
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 370-376
    • Ikebe, M.1    Brozovich, F.V.2
  • 15
    • 0033214346 scopus 로고    scopus 로고
    • 2+ sensitization in triton X-100-demembranated rabbit arterial smooth muscle
    • 2+ sensitization in triton X-100-demembranated rabbit arterial smooth muscle. J. Physiol. 520, 139-152
    • (1999) J. Physiol. , vol.520 , pp. 139-152
    • Kitazawa, T.1    Takizawa, N.2    Ikebe, M.3    Eto, M.4
  • 16
    • 0029583638 scopus 로고
    • A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization
    • Eto, M., Ohmori, T., Suzuki, M., Furuya, K. and Morita, F. (1995) A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization. J. Biochem. (Tokyo) 118, 1104-1107
    • (1995) J. Biochem. (Tokyo) , vol.118 , pp. 1104-1107
    • Eto, M.1    Ohmori, T.2    Suzuki, M.3    Furuya, K.4    Morita, F.5
  • 17
    • 0031920581 scopus 로고    scopus 로고
    • Possible involvement of the novel CPI-17 protein in protein kinase C signal transduction of rabbit arterial smooth muscle
    • Li, L., Eto, M., Lee, M. R., Morita, F., Yazawa, M. and Kitazawa, T. (1998) Possible involvement of the novel CPI-17 protein in protein kinase C signal transduction of rabbit arterial smooth muscle. J. Physiol. 508, 871-881
    • (1998) J. Physiol. , vol.508 , pp. 871-881
    • Li, L.1    Eto, M.2    Lee, M.R.3    Morita, F.4    Yazawa, M.5    Kitazawa, T.6
  • 18
    • 0034616292 scopus 로고    scopus 로고
    • Agonists trigger G protein-mediated activation of the CPI-17 inhibitor phosphoprotein of myosin light chain phosphatase to enhance vascular smooth muscle contractility
    • Kitazawa, T., Eto, M., Woodsome, T. P. and Brautigan, D. L. (2000) Agonists trigger G protein-mediated activation of the CPI-17 inhibitor phosphoprotein of myosin light chain phosphatase to enhance vascular smooth muscle contractility. J. Biol. Chem. 275, 9897-9900
    • (2000) J. Biol. Chem. , vol.275 , pp. 9897-9900
    • Kitazawa, T.1    Eto, M.2    Woodsome, T.P.3    Brautigan, D.L.4
  • 23
    • 0029831696 scopus 로고    scopus 로고
    • Role of Rho proteins in carbachol-induced contractions in intact and permeabilized guinea-pig intestinal smooth muscle
    • Otto, B., Steusloff, A., Just, I., Aktories, K. and Pfitzer, G. (1996) Role of Rho proteins in carbachol-induced contractions in intact and permeabilized guinea-pig intestinal smooth muscle. J. Physiol. 496, 317-329
    • (1996) J. Physiol. , vol.496 , pp. 317-329
    • Otto, B.1    Steusloff, A.2    Just, I.3    Aktories, K.4    Pfitzer, G.5
  • 24
    • 0027049145 scopus 로고
    • The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1
    • Alessi, D., MacDougall, L. K., Sola, M. M., Ikebe, M. and Cohen, P. (1992) The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1. Eur. J. Biochem. 210, 1023-1035
    • (1992) Eur. J. Biochem. , vol.210 , pp. 1023-1035
    • Alessi, D.1    MacDougall, L.K.2    Sola, M.M.3    Ikebe, M.4    Cohen, P.5
  • 25
    • 0028152923 scopus 로고
    • Purification and characterization of the mammalian myosin light chain phosphatase holoenzyme. The differential effects of the holoenzyme and its subunits on smooth muscle
    • Shirazi, A., Iizuka, K., Fadden, P., Mosse, C., Somlyo, A. P., Somlyo, A. V. and Haystead, T. A. (1994) Purification and characterization of the mammalian myosin light chain phosphatase holoenzyme. The differential effects of the holoenzyme and its subunits on smooth muscle. J. Biol. Chem. 269, 31598-31606
    • (1994) J. Biol. Chem. , vol.269 , pp. 31598-31606
    • Shirazi, A.1    Iizuka, K.2    Fadden, P.3    Mosse, C.4    Somlyo, A.P.5    Somlyo, A.V.6    Haystead, T.A.7
  • 28
    • 0033601250 scopus 로고    scopus 로고
    • Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase
    • Feng, J., Ito, M., Ichikawa, K., Isaka, N., Nishikawa, M., Hartshorne, D. J. and Nakano, T. (1999) Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase. J. Biol. Chem. 274, 37385-37390
    • (1999) J. Biol. Chem. , vol.274 , pp. 37385-37390
    • Feng, J.1    Ito, M.2    Ichikawa, K.3    Isaka, N.4    Nishikawa, M.5    Hartshorne, D.J.6    Nakano, T.7
  • 30
    • 0033955903 scopus 로고    scopus 로고
    • Rho kinase inhibitor HA-1077 prevents Rho-mediated myosin phosphatase inhibition in smooth muscle cells
    • Nagumo, H., Sasaki, Y., Ono, Y., Okamoto, H., Seto, M. and Takuwa, Y. (2000) Rho kinase inhibitor HA-1077 prevents Rho-mediated myosin phosphatase inhibition in smooth muscle cells. Am. J. Physiol. Cell. Physiol. 278, C57-C65
    • (2000) Am. J. Physiol. Cell. Physiol. , vol.278
    • Nagumo, H.1    Sasaki, Y.2    Ono, Y.3    Okamoto, H.4    Seto, M.5    Takuwa, Y.6
  • 31
    • 0027938294 scopus 로고
    • Structural requirement of the regulatory light chain of smooth muscle myosin as a substrate for myosin light chain kinase
    • Ikebe, M., Reardon, S., Schwonek, J. P., Sanders, C. R. and Ikebe, R. (1994) Structural requirement of the regulatory light chain of smooth muscle myosin as a substrate for myosin light chain kinase. J. Biol. Chem. 269, 28165-28172
    • (1994) J. Biol. Chem. , vol.269 , pp. 28165-28172
    • Ikebe, M.1    Reardon, S.2    Schwonek, J.P.3    Sanders, C.R.4    Ikebe, R.5
  • 32
    • 0032504192 scopus 로고    scopus 로고
    • A hinge at the central helix of the regulatory light chain of myosin is critical for phosphorylation-dependent regulation of smooth muscle myosin motor activity
    • Ikebe, M., Kambara, T., Stafford, W. F., Sata, M., Katayama, E. and Ikebe, R. (1998) A hinge at the central helix of the regulatory light chain of myosin is critical for phosphorylation-dependent regulation of smooth muscle myosin motor activity. J. Biol. Chem. 273, 17702-17707
    • (1998) J. Biol. Chem. , vol.273 , pp. 17702-17707
    • Ikebe, M.1    Kambara, T.2    Stafford, W.F.3    Sata, M.4    Katayama, E.5    Ikebe, R.6
  • 33
    • 0034602428 scopus 로고    scopus 로고
    • Effects of the regulatory light chain phosphorylation of myosin II on mitosis and cytokinesis of mammalian cells
    • Komatsu, S., Yano, T., Shibata, M., Tuft, R. A. and Ikebe, M. (2000) Effects of the regulatory light chain phosphorylation of myosin II on mitosis and cytokinesis of mammalian cells. J. Biol. Chem. 275, 34512-34520
    • (2000) J. Biol. Chem. , vol.275 , pp. 34512-34520
    • Komatsu, S.1    Yano, T.2    Shibata, M.3    Tuft, R.A.4    Ikebe, M.5
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0024516275 scopus 로고
    • Inhibition of conformational change in smooth muscle myosin by a monoclonal antibody against the 17-kDa light chain
    • Highashihara, M., Frado, L. L., Craig, R. and Ikebe, M. (1989) Inhibition of conformational change in smooth muscle myosin by a monoclonal antibody against the 17-kDa light chain. J. Biol. Chem. 264, 5218-5225
    • (1989) J. Biol. Chem. , vol.264 , pp. 5218-5225
    • Highashihara, M.1    Frado, L.L.2    Craig, R.3    Ikebe, M.4
  • 36
    • 0035800812 scopus 로고    scopus 로고
    • Histamine-induced vasoconstriction involves phosphorylation of a specific inhibitor protein for myosin phosphatase by protein kinase C α and δ isoforms
    • Eto, M., Kitazawa, T., Yazawa, M., Mukai, H., Ono, Y. and Brautigan, D. L. (2001) Histamine-induced vasoconstriction involves phosphorylation of a specific inhibitor protein for myosin phosphatase by protein kinase C α and δ isoforms. J. Biol. Chem. 276, 29072-29078
    • (2001) J. Biol. Chem. , vol.276 , pp. 29072-29078
    • Eto, M.1    Kitazawa, T.2    Yazawa, M.3    Mukai, H.4    Ono, Y.5    Brautigan, D.L.6
  • 37
    • 0034705765 scopus 로고    scopus 로고
    • Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase
    • Koyama, M., Ito, M., Feng, J., Seko, T., Shiraki, K., Takase, K., Hartshorne, D. J. and Nakano, T. (2000) Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase. FEBS Lett. 475, 197-200
    • (2000) FEBS Lett. , vol.475 , pp. 197-200
    • Koyama, M.1    Ito, M.2    Feng, J.3    Seko, T.4    Shiraki, K.5    Takase, K.6    Hartshorne, D.J.7    Nakano, T.8
  • 38
    • 0024465081 scopus 로고
    • Molecular biology and biochemistry of the endothelins
    • Yanagisawa, M. and Masaki, T. (1989) Molecular biology and biochemistry of the endothelins. Trends Pharmacol. Sci. 10, 374-378
    • (1989) Trends Pharmacol. Sci. , vol.10 , pp. 374-378
    • Yanagisawa, M.1    Masaki, T.2
  • 40
    • 0023655566 scopus 로고
    • Phosphorylation of the 20,000-dalton light chain of smooth muscle myosin by the calcium-activated, phospholipid-dependent protein kinase. Phosphorylation sites and effects of phosphorylation
    • Ikebe, M., Hartshorne, D. J. and Elzinga, M. (1987) Phosphorylation of the 20,000-dalton light chain of smooth muscle myosin by the calcium-activated, phospholipid-dependent protein kinase. Phosphorylation sites and effects of phosphorylation. J. Biol. Chem. 262, 9569-9573
    • (1987) J. Biol. Chem. , vol.262 , pp. 9569-9573
    • Ikebe, M.1    Hartshorne, D.J.2    Elzinga, M.3
  • 42
    • 0035877985 scopus 로고    scopus 로고
    • Protein kinase C-catalyzed phosphorylation of an inhibitory phosphoprotein of myosin phosphatase is involved in human platelet secretion
    • Watanabe, Y., Ito, M., Kataoka, Y., Wada, H., Koyama, M., Feng, J., Shiku, H. and Nishikawa, M. (2001) Protein kinase C-catalyzed phosphorylation of an inhibitory phosphoprotein of myosin phosphatase is involved in human platelet secretion. Blood 97, 3798-3805
    • (2001) Blood , vol.97 , pp. 3798-3805
    • Watanabe, Y.1    Ito, M.2    Kataoka, Y.3    Wada, H.4    Koyama, M.5    Feng, J.6    Shiku, H.7    Nishikawa, M.8
  • 45
    • 0037155782 scopus 로고    scopus 로고
    • Differential association and localization of myosin phosphatase subunits during agonist-induced signal transduction in smooth muscle
    • Shin, H. M., Je, H. D., Gallant, C., Tao, T. C., Hartshorne, D. J., Ito, M. and Morgan, K. G. (2002) Differential association and localization of myosin phosphatase subunits during agonist-induced signal transduction in smooth muscle. Circ. Res. 90, 546-553
    • (2002) Circ. Res. , vol.90 , pp. 546-553
    • Shin, H.M.1    Je, H.D.2    Gallant, C.3    Tao, T.C.4    Hartshorne, D.J.5    Ito, M.6    Morgan, K.G.7
  • 46
    • 0037181495 scopus 로고    scopus 로고
    • Dephosphorylation of the two regulatory components of myosin phosphatase. MBS and CPI17
    • Takizawa, N., Niiro, N. and Ikebe, M. (2002) Dephosphorylation of the two regulatory components of myosin phosphatase. MBS and CPI17. FEBS Lett. 515, 127-132
    • (2002) FEBS Lett. , vol.515 , pp. 127-132
    • Takizawa, N.1    Niiro, N.2    Ikebe, M.3
  • 47
    • 0035933870 scopus 로고    scopus 로고
    • Protein kinase C-α signals rhoguanine nucleotide dissociation inhibitor phosphorylation and rho activation and regulates the endothelial cell barrier function
    • Mehta, D., Rahman, A. and Malik, A. B. (2001) Protein kinase C-α signals rhoguanine nucleotide dissociation inhibitor phosphorylation and rho activation and regulates the endothelial cell barrier function. J. Biol. Chem. 276, 22614-22620
    • (2001) J. Biol. Chem. , vol.276 , pp. 22614-22620
    • Mehta, D.1    Rahman, A.2    Malik, A.B.3
  • 48
    • 0034698841 scopus 로고    scopus 로고
    • Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibres and focal adhesions in 3T3 fibroblasts
    • Totsukawa, G., Yamakita, Y., Yamashiro, S., Hartshorne, D. J., Sasaki, Y. and Matsumura, F. (2000) Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibres and focal adhesions in 3T3 fibroblasts. J. Cell. Biol. 150, 797-806
    • (2000) J. Cell. Biol. , vol.150 , pp. 797-806
    • Totsukawa, G.1    Yamakita, Y.2    Yamashiro, S.3    Hartshorne, D.J.4    Sasaki, Y.5    Matsumura, F.6


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